Structure-function analysis of the 7B2 CT peptide

Structure-function analysis of the 7B2 CT peptide

Autor Apletalina, E. V. Google Scholar
Juliano, M. A. Google Scholar
Juliano, L. Google Scholar
Lindberg, I Google Scholar
Instituição Louisiana State Univ
Universidade Federal de São Paulo (UNIFESP)
Resumo Prohormone convertases play important roles in the proteolytic conversion of many protein precursors. the neuroendocrine protein 7B2 and its 31-residue carboxyl-terminal (CT) peptide potently and specifically inhibit prohormone convertase 2 (PC2), We have analyzed the residues contributing to inhibition using N-terminal truncation and alanine scanning. Removal of more than 3 residues from the amino-terminal end of CT1-18 resulted in a more than 190-fold drop in inhibitory activity, showing that most of the residues between 3 and 18 are required for inhibition. in agreement, an Ala scan indicated that only 4 residues could be replaced with Ala without losing mid-nanomolar inhibitory: potency; in particular, Gln7, Gln9, and Asp12 could be Ala-substituted to yield peptides with a similar inhibitory potency to the starting peptide. the all-D-retro-inverso, all-L-inverso, and all-D analogues of CT peptide were completely inactive, indicating that amino acid side chains and the CT peptide main chain interact with PC2, CT peptide inhibition could not be competitively blocked by preincubation with truncated CT peptide forms, supporting an absolute requirement for the Lys-Lys pair in initial binding of the CT peptide to the active site, (C) 2000 Academic Press.
Idioma Inglês
Data de publicação 2000-01-27
Publicado em Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc, v. 267, n. 3, p. 940-942, 2000.
ISSN 0006-291X (Sherpa/Romeo, fator de impacto)
Publicador Academic Press Inc
Extensão 940-942
Fonte http://dx.doi.org/10.1006/bbrc.1999.2060
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000085131800045
Endereço permanente http://repositorio.unifesp.br/handle/11600/26238

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